| + |
SRC | up-regulates activity 
phosphorylation
|
CTNND2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278326 |
Tyr1154 |
QEPSRKDyETYQPFQ |
Homo sapiens |
|
| pmid |
sentence |
| 24412473 |
Furthermore, according to our data from immunoprecipitation to py20 antibody, c-Src can phosphorylate delta-catenin on Y1073, Y1176, Y1179 and Y1112, with the predominant sites being Y1073, Y1112 and Y1176.|Interestingly, we found that c-Src can increase the stability of delta-catenin in MEF cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278327 |
Tyr1157 |
SRKDYETyQPFQNST |
Homo sapiens |
|
| pmid |
sentence |
| 24412473 |
Furthermore, according to our data from immunoprecipitation to py20 antibody, c-Src can phosphorylate delta-catenin on Y1073, Y1176, Y1179 and Y1112, with the predominant sites being Y1073, Y1112 and Y1176.|Interestingly, we found that c-Src can increase the stability of delta-catenin in MEF cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HES1 | down-regulates quantity by repression 
transcriptional regulation
|
CTNND2 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251877 |
|
|
Mus musculus |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 21106062 |
Coordinated regulation of δ-catenin expression by both the activating transcription factor E2F1 and repressive transcription factor Hes1 in prostate cancer progression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH3 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252130 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
E2F1 | up-regulates quantity by expression 
transcriptional regulation
|
CTNND2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251876 |
|
|
Mus musculus |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 21106062 |
Coordinated regulation of δ-catenin expression by both the activating transcription factor E2F1 and repressive transcription factor Hes1 in prostate cancer progression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH2 |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252131 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity
phosphorylation
|
CTNND2 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279323 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20573893 |
Cdk5 mediated delta-catenin phosphorylation regulates delta-catenin subcellular localization into two distinct pools : a cytoplasmic or intraneurite state as well as a pool that is localized to the membrane.|Cdk5 phosphorylates delta-catenin on serines 300 and 357. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH1 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252134 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND2 | up-regulates activity
binding
|
ERBIN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252120 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11821434 |
We characterized the interactions between the Erbin PDZ domain and both ARVCF and δ-catenin in vitro and in vivo. endogenous δ-catenin and Erbin co-localized in and co-immunoprecipitated from neurons. These results suggest that δ-catenin and ARVCF may function to mediate the association of Erbin with the junctional cadherin-catenin complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH5 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252132 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAX6 | up-regulates quantity by expression
transcriptional regulation
|
CTNND2 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251878 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16973151 |
In Pax6 mutant embryos, delta-catenin expression was severely reduced in the optic vesicle neural ectoderm, in the ventricular zone of the neocortex and in the external granule layer of the cerebellum. We identified a Pax6 binding site in delta-catenin promoter that is conserved between mice and humans and which is effectively bound by Pax6 in vitro. Our results suggest that Pax6 regulates delta-catenin expression during CNS development in mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GSK3B | down-regulates quantity 
phosphorylation
|
CTNND2 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279719 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20623542 |
Therefore, our data which supports that partial inhibition of GSK-3beta increases delta-catenin expression, raises an interesting possibility that delta-catenin may be an important downstream target of GSK-3beta signaling that participates in modulating neuronal morphology.|We demonstrate that GSK-3beta forms a stable complex with delta-catenin and phosphorylates delta-catenin in neurons, an event that mediates ubiquitination and subsequent proteasome degradation of delta-catenin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CTNND2
- 
- 